人5-氨基乙酰丙酸脱水酶活性位点赖氨酸的鉴定。
Identification of lysine at the active site of human 5-aminolaevulinate dehydratase.
作者信息
Gibbs P N, Jordan P M
出版信息
Biochem J. 1986 Jun 1;236(2):447-51. doi: 10.1042/bj2360447.
Abstract
Reduction of human 5-aminolaevulinate dehydratase with NaBH4 in the presence of 14C-labelled substrate led to complete loss of catalytic activity and to incorporation of label into the enzyme protein. By comparison with authentic lysyl-aminolaevulinic acid, prepared chemically, the modified active-site amino acid obtained by acid hydrolysis was shown to be lysine. Sequencing of a CNBr-cleavage peptide isolated from the inactivated 14C-labelled enzyme revealed that the lysine was present within the sequence M-V-K-P-G-M.
摘要
在含有¹⁴C标记底物的情况下，用硼氢化钠还原人5-氨基乙酰丙酸脱水酶，导致催化活性完全丧失，并使标记物掺入酶蛋白中。通过与化学合成的真实赖氨酰-氨基乙酰丙酸进行比较，经酸水解得到的修饰活性位点氨基酸被证明是赖氨酸。对从失活的¹⁴C标记酶中分离出的溴化氰裂解肽进行测序，结果显示赖氨酸存在于序列M-V-K-P-G-M中。
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